[HTML][HTML] The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1
A Freywald, N Sharfe, CM Roifman - Journal of Biological Chemistry, 2002 - ASBMB
Uniquely for the Eph family of receptor tyrosine kinases, the EphB6 receptor is catalytically
inactive due to the alteration of several critical residues in its kinase domain. This has cast
doubt upon its ability to participate in cytoplasmic signaling events. We show here that
despite its lack of kinase activity, EphB6 undergoes inducible tyrosine phosphorylation upon
stimulation with the Eph-B receptor subfamily ligand ephrin-B1. We also demonstrate, for the
first time, evidence of cross-talk between Eph receptors. Overexpression of a catalytically …
inactive due to the alteration of several critical residues in its kinase domain. This has cast
doubt upon its ability to participate in cytoplasmic signaling events. We show here that
despite its lack of kinase activity, EphB6 undergoes inducible tyrosine phosphorylation upon
stimulation with the Eph-B receptor subfamily ligand ephrin-B1. We also demonstrate, for the
first time, evidence of cross-talk between Eph receptors. Overexpression of a catalytically …
